ID GALT3_HUMAN Reviewed; 633 AA. AC Q14435; Q53TG9; Q7Z476; DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 14-OCT-2008, sequence version 2. DT 27-MAR-2024, entry version 196. DE RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 3; DE EC=2.4.1.41 {ECO:0000269|PubMed:16638743, ECO:0000269|PubMed:31932717, ECO:0000269|PubMed:8663203, ECO:0000269|PubMed:9295285}; DE AltName: Full=Polypeptide GalNAc transferase 3; DE Short=GalNAc-T3; DE Short=pp-GaNTase 3; DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase 3; DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3; GN Name=GALNT3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, AND RP TISSUE SPECIFICITY. RC TISSUE=Salivary gland; RX PubMed=8663203; DOI=10.1074/jbc.271.29.17006; RA Bennett E.P., Hassan H., Clausen H.; RT "cDNA cloning and expression of a novel human UDP-N-acetyl-alpha-D- RT galactosamine polypeptide N-acetylgalactosaminyltransferase, GalNAc-T3."; RL J. Biol. Chem. 271:17006-17012(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR. RX PubMed=9295285; DOI=10.1074/jbc.272.38.23503; RA Wandall H.H., Hassan H., Mirgorodskaya E., Kristensen A.K., Roepstorff P., RA Bennett E.P., Nielsen P.A., Hollingsworth M.A., Burchell J., RA Taylor-Papadimitriou J., Clausen H.; RT "Substrate specificities of three members of the human UDP-N-acetyl-alpha- RT D-galactosamine:polypeptide N-acetylgalactosaminyltransferase family, RT GalNAc-T1, -T2, and -T3."; RL J. Biol. Chem. 272:23503-23514(1997). RN [6] RP SUBCELLULAR LOCATION. RX PubMed=9394011; DOI=10.1242/jcs.111.1.45; RA Roettger S., White J., Wandall H.H., Olivo J.-C., Stark A., Bennett E.P., RA Whitehouse C., Berger E.G., Clausen H., Nilsson T.; RT "Localization of three human polypeptide GalNAc-transferases in HeLa cells RT suggests initiation of O-linked glycosylation throughout the Golgi RT apparatus."; RL J. Cell Sci. 111:45-60(1998). RN [7] RP TISSUE SPECIFICITY. RX PubMed=12708471; DOI=10.1111/j.1349-7006.2003.tb01348.x; RA Onitsuka K., Shibao K., Nakayama Y., Minagawa N., Hirata K., Izumi H., RA Matsuo K., Nagata N., Kitazato K., Kohno K., Itoh H.; RT "Prognostic significance of UDP-N-acetyl-alpha-D-galactosamine:polypeptide RT N-acetylgalactosaminyltransferase-3 (GalNAc-T3) expression in patients with RT gastric carcinoma."; RL Cancer Sci. 94:32-36(2003). RN [8] RP INVOLVEMENT IN HFTC1, AND VARIANT HFTC 162-ARG--ASP-633 DEL. RX PubMed=15133511; DOI=10.1038/ng1358; RA Topaz O., Shurman D.L., Bergman R., Indelman M., Ratajczak P., Mizrachi M., RA Khamaysi Z., Behar D., Petronius D., Friedman V., Zelikovic I., Raimer S., RA Metzker A., Richard G., Sprecher E.; RT "Mutations in GALNT3, encoding a protein involved in O-linked RT glycosylation, cause familial tumoral calcinosis."; RL Nat. Genet. 36:579-581(2004). RN [9] RP INVOLVEMENT IN HFTC1. RX PubMed=15599692; DOI=10.1007/s00109-004-0610-8; RA Frishberg Y., Topaz O., Bergman R., Behar D., Fisher D., Gordon D., RA Richard G., Sprecher E.; RT "Identification of a recurrent mutation in GALNT3 demonstrates that RT hyperostosis-hyperphosphatemia syndrome and familial tumoral calcinosis are RT allelic disorders."; RL J. Mol. Med. 83:33-38(2005). RN [10] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=16638743; DOI=10.1074/jbc.m602469200; RA Kato K., Jeanneau C., Tarp M.A., Benet-Pages A., Lorenz-Depiereux B., RA Bennett E.P., Mandel U., Strom T.M., Clausen H.; RT "Polypeptide GalNAc-transferase T3 and familial tumoral calcinosis. RT Secretion of fibroblast growth factor 23 requires O-glycosylation."; RL J. Biol. Chem. 281:18370-18377(2006). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [12] RP X-RAY SCATTERING SOLUTION STRUCTURE, FUNCTION, CATALYTIC ACTIVITY, RP BIOPHYSICOCHEMICAL PROPERTIES, RICIN B-TYPE LECTIN DOMAIN, AND MUTAGENESIS RP OF ASP-277; 510-LYS--ASP-633 AND ASP-519. RX PubMed=31932717; DOI=10.1038/s41589-019-0444-x; RA de Las Rivas M., Paul Daniel E.J., Narimatsu Y., Companon I., Kato K., RA Hermosilla P., Thureau A., Ceballos-Laita L., Coelho H., Bernado P., RA Marcelo F., Hansen L., Maeda R., Lostao A., Corzana F., Clausen H., RA Gerken T.A., Hurtado-Guerrero R.; RT "Molecular basis for fibroblast growth factor 23 O-glycosylation by GalNAc- RT T3."; RL Nat. Chem. Biol. 16:351-360(2020). CC -!- FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide CC biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a CC serine or threonine residue on the protein receptor (PubMed:8663203, CC PubMed:9295285, PubMed:16638743, PubMed:31932717). Has activity toward CC HIV envelope glycoprotein gp120, EA2, MUC2, MUC1A and MUC5AC CC (PubMed:8663203, PubMed:9295285). Probably glycosylates fibronectin in CC vivo (PubMed:9295285). Glycosylates FGF23 (PubMed:16638743, CC PubMed:31932717). {ECO:0000269|PubMed:16638743, CC ECO:0000269|PubMed:31932717, ECO:0000269|PubMed:8663203, CC ECO:0000269|PubMed:9295285}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O- CC [N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + H(+) + UDP; CC Xref=Rhea:RHEA:23956, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:12788, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:53604, CC ChEBI:CHEBI:58223, ChEBI:CHEBI:67138; EC=2.4.1.41; CC Evidence={ECO:0000269|PubMed:8663203, ECO:0000269|PubMed:9295285}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-threonyl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3- CC O-[N-acetyl-alpha-D-galactosaminyl]-L-threonyl-[protein] + H(+) + CC UDP; Xref=Rhea:RHEA:52424, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:58223, CC ChEBI:CHEBI:67138, ChEBI:CHEBI:87075; EC=2.4.1.41; CC Evidence={ECO:0000269|PubMed:16638743, ECO:0000269|PubMed:31932717, CC ECO:0000269|PubMed:8663203, ECO:0000269|PubMed:9295285}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000269|PubMed:9295285}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=36 uM for FGF23 NAPIPRRHTRSAEDDS peptide CC {ECO:0000269|PubMed:31932717}; CC KM=423 uM for FGF23 HFNTPIPRRH peptide {ECO:0000269|PubMed:31932717}; CC KM=0.5 mM for MUC1A APPAHGVTSAPDTRPAPGC peptide CC {ECO:0000269|PubMed:9295285}; CC KM=0.1 mM for MUC2 PTTTPISTTTMVTPTPTPTC peptide CC {ECO:0000269|PubMed:9295285}; CC -!- PATHWAY: Protein modification; protein glycosylation. CC -!- INTERACTION: CC Q14435-2; Q92624: APPBP2; NbExp=3; IntAct=EBI-10232904, EBI-743771; CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane CC {ECO:0000269|PubMed:9394011}; Single-pass type II membrane protein CC {ECO:0000269|PubMed:9394011}. Note=Resides preferentially in the trans CC and medial parts of the Golgi stack. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q14435-1; Sequence=Displayed; CC Name=2; CC IsoId=Q14435-2; Sequence=VSP_011202, VSP_011203; CC -!- TISSUE SPECIFICITY: Expressed in organs that contain secretory CC epithelial glands. Highly expressed in pancreas, skin, kidney and CC testis. Weakly expressed in prostate, ovary, intestine and colon. Also CC expressed in placenta and lung and fetal lung and fetal kidney. CC {ECO:0000269|PubMed:12708471, ECO:0000269|PubMed:8663203}. CC -!- DOMAIN: There are two conserved domains in the glycosyltransferase CC region: the N-terminal domain (domain A, also called GT1 motif), which CC is probably involved in manganese coordination and substrate binding CC and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), CC which is probably involved in catalytic reaction and UDP-Gal binding. CC {ECO:0000250|UniProtKB:O08912}. CC -!- DOMAIN: The ricin B-type lectin domain binds to GalNAc and contributes CC to the glycopeptide specificity (By similarity). Essential for CC glycosylation of FGF23 (PubMed:31932717). CC {ECO:0000250|UniProtKB:Q8N4A0, ECO:0000269|PubMed:31932717}. CC -!- DISEASE: Tumoral calcinosis, hyperphosphatemic, familial, 1 (HFTC1) CC [MIM:211900]: A form of hyperphosphatemic tumoral calcinosis, a rare CC autosomal recessive metabolic disorder that manifests with CC hyperphosphatemia and massive calcium deposits in the skin and CC subcutaneous tissues. Some patients have recurrent, transient, painful CC swellings of the long bones associated with the radiographic findings CC of periosteal reaction and cortical hyperostosis and absence of skin CC involvement. {ECO:0000269|PubMed:15133511, CC ECO:0000269|PubMed:15599692}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- MISCELLANEOUS: Overexpressed in many differentiated carcinomas, CC suggesting that it may serve as a marker of tumor differentiation. CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T CC subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH56246.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; CC Note=Polypeptide N-acetylgalactosaminyltransferase 3; CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_485"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X92689; CAA63371.1; -; mRNA. DR EMBL; AC009495; AAY14678.1; -; Genomic_DNA. DR EMBL; CH471058; EAX11324.1; -; Genomic_DNA. DR EMBL; BC056246; AAH56246.1; ALT_INIT; mRNA. DR EMBL; BC113565; AAI13566.1; -; mRNA. DR EMBL; BC113567; AAI13568.1; -; mRNA. DR CCDS; CCDS2226.1; -. [Q14435-1] DR RefSeq; NP_004473.2; NM_004482.3. [Q14435-1] DR RefSeq; XP_005246506.1; XM_005246449.1. [Q14435-1] DR RefSeq; XP_011509231.1; XM_011510929.1. [Q14435-1] DR RefSeq; XP_016859259.1; XM_017003770.1. [Q14435-1] DR AlphaFoldDB; Q14435; -. DR SMR; Q14435; -. DR BioGRID; 108863; 26. DR IntAct; Q14435; 6. DR STRING; 9606.ENSP00000376465; -. DR BindingDB; Q14435; -. DR ChEMBL; CHEMBL4523291; -. DR CAZy; CBM13; Carbohydrate-Binding Module Family 13. DR CAZy; GT27; Glycosyltransferase Family 27. DR GlyConnect; 1620; 3 N-Linked glycans (1 site). DR GlyCosmos; Q14435; 3 sites, 3 glycans. DR GlyGen; Q14435; 6 sites, 3 N-linked glycans (1 site), 1 O-linked glycan (3 sites). DR iPTMnet; Q14435; -. DR PhosphoSitePlus; Q14435; -. DR SwissPalm; Q14435; -. DR BioMuta; GALNT3; -. DR DMDM; 209572629; -. DR EPD; Q14435; -. DR jPOST; Q14435; -. DR MassIVE; Q14435; -. DR MaxQB; Q14435; -. DR PaxDb; 9606-ENSP00000376465; -. DR PeptideAtlas; Q14435; -. DR ProteomicsDB; 59988; -. [Q14435-1] DR ProteomicsDB; 59989; -. [Q14435-2] DR Pumba; Q14435; -. DR Antibodypedia; 2358; 196 antibodies from 25 providers. DR DNASU; 2591; -. DR Ensembl; ENST00000392701.8; ENSP00000376465.3; ENSG00000115339.14. [Q14435-1] DR GeneID; 2591; -. DR KEGG; hsa:2591; -. DR MANE-Select; ENST00000392701.8; ENSP00000376465.3; NM_004482.4; NP_004473.2. DR UCSC; uc010fph.2; human. [Q14435-1] DR AGR; HGNC:4125; -. DR CTD; 2591; -. DR DisGeNET; 2591; -. DR GeneCards; GALNT3; -. DR GeneReviews; GALNT3; -. DR HGNC; HGNC:4125; GALNT3. DR HPA; ENSG00000115339; Tissue enhanced (stomach). DR MalaCards; GALNT3; -. DR MIM; 211900; phenotype. DR MIM; 601756; gene. DR neXtProt; NX_Q14435; -. DR OpenTargets; ENSG00000115339; -. DR Orphanet; 306661; Familial hyperphosphatemic tumoral calcinosis/Hyperphosphatemic hyperostosis syndrome. DR PharmGKB; PA28538; -. DR VEuPathDB; HostDB:ENSG00000115339; -. DR eggNOG; KOG3736; Eukaryota. DR GeneTree; ENSGT00940000156609; -. DR InParanoid; Q14435; -. DR OMA; NPLFKMC; -. DR OrthoDB; 202750at2759; -. DR PhylomeDB; Q14435; -. DR TreeFam; TF313267; -. DR BRENDA; 2.4.1.41; 2681. DR PathwayCommons; Q14435; -. DR Reactome; R-HSA-190372; FGFR3c ligand binding and activation. DR Reactome; R-HSA-5083625; Defective GALNT3 causes HFTC. DR Reactome; R-HSA-913709; O-linked glycosylation of mucins. DR SignaLink; Q14435; -. DR UniPathway; UPA00378; -. DR BioGRID-ORCS; 2591; 11 hits in 1145 CRISPR screens. DR ChiTaRS; GALNT3; human. DR GeneWiki; GALNT3; -. DR GenomeRNAi; 2591; -. DR Pharos; Q14435; Tbio. DR PRO; PR:Q14435; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q14435; Protein. DR Bgee; ENSG00000115339; Expressed in mucosa of sigmoid colon and 149 other cell types or tissues. DR ExpressionAtlas; Q14435; baseline and differential. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA. DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0016020; C:membrane; TAS:ProtInc. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL. DR GO; GO:0005509; F:calcium ion binding; IDA:BHF-UCL. DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW. DR GO; GO:0030145; F:manganese ion binding; IDA:BHF-UCL. DR GO; GO:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; IDA:UniProtKB. DR GO; GO:0005975; P:carbohydrate metabolic process; NAS:ProtInc. DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; TAS:Reactome. DR GO; GO:0016266; P:O-glycan processing; TAS:Reactome. DR GO; GO:0006493; P:protein O-linked glycosylation; IDA:UniProtKB. DR GO; GO:0018242; P:protein O-linked glycosylation via serine; IDA:BHF-UCL. DR GO; GO:0018243; P:protein O-linked glycosylation via threonine; IDA:UniProtKB. DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl. DR CDD; cd02510; pp-GalNAc-T; 1. DR CDD; cd00161; RICIN; 1. DR Gene3D; 2.80.10.50; -; 1. DR InterPro; IPR045885; GalNAc-T. DR InterPro; IPR001173; Glyco_trans_2-like. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR InterPro; IPR035992; Ricin_B-like_lectins. DR InterPro; IPR000772; Ricin_B_lectin. DR PANTHER; PTHR11675; N-ACETYLGALACTOSAMINYLTRANSFERASE; 1. DR PANTHER; PTHR11675:SF33; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 3; 1. DR Pfam; PF00535; Glycos_transf_2; 1. DR Pfam; PF00652; Ricin_B_lectin; 1. DR SMART; SM00458; RICIN; 1. DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1. DR SUPFAM; SSF50370; Ricin B-like lectins; 1. DR PROSITE; PS50231; RICIN_B_LECTIN; 1. DR Genevisible; Q14435; HS. PE 1: Evidence at protein level; KW Alternative splicing; Disease variant; Disulfide bond; Glycoprotein; KW Glycosyltransferase; Golgi apparatus; Lectin; Manganese; Membrane; KW Metal-binding; Reference proteome; Signal-anchor; Transferase; KW Transmembrane; Transmembrane helix. FT CHAIN 1..633 FT /note="Polypeptide N-acetylgalactosaminyltransferase 3" FT /id="PRO_0000059106" FT TOPO_DOM 1..19 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 20..37 FT /note="Helical; Signal-anchor for type II membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 38..633 FT /note="Lumenal" FT /evidence="ECO:0000255" FT DOMAIN 504..630 FT /note="Ricin B-type lectin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174" FT REGION 184..293 FT /note="Catalytic subdomain A" FT REGION 356..418 FT /note="Catalytic subdomain B" FT BINDING 277 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000250|UniProtKB:H0ZAB5" FT BINDING 279 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000250|UniProtKB:H0ZAB5" FT BINDING 415 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000250|UniProtKB:H0ZAB5" FT BINDING 519 FT /ligand="UDP-N-acetyl-alpha-D-galactosamine" FT /ligand_id="ChEBI:CHEBI:67138" FT /evidence="ECO:0000250|UniProtKB:H0ZAB5" FT BINDING 522 FT /ligand="UDP-N-acetyl-alpha-D-galactosamine" FT /ligand_id="ChEBI:CHEBI:67138" FT /evidence="ECO:0000250|UniProtKB:H0ZAB5" FT BINDING 536 FT /ligand="UDP-N-acetyl-alpha-D-galactosamine" FT /ligand_id="ChEBI:CHEBI:67138" FT /evidence="ECO:0000250|UniProtKB:H0ZAB5" FT BINDING 541 FT /ligand="UDP-N-acetyl-alpha-D-galactosamine" FT /ligand_id="ChEBI:CHEBI:67138" FT /evidence="ECO:0000250|UniProtKB:H0ZAB5" FT CARBOHYD 132 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 297 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 484 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 517..535 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174" FT DISULFID 561..574 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174" FT DISULFID 605..618 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174" FT VAR_SEQ 173..192 FT /note="CIEQKFKRCPPLPTTSVIIV -> YVEEYLLFILYHQALQGREG (in FT isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_011202" FT VAR_SEQ 193..633 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_011203" FT VARIANT 162..633 FT /note="Missing (in HFTC1)" FT /evidence="ECO:0000269|PubMed:15133511" FT /id="VAR_080832" FT MUTAGEN 277 FT /note="D->H: Loss of ability to glycosylate FGF23." FT /evidence="ECO:0000269|PubMed:31932717" FT MUTAGEN 510..633 FT /note="Missing: Loss of ability to glycosylate FGF23." FT /evidence="ECO:0000269|PubMed:31932717" FT MUTAGEN 519 FT /note="D->H: Loss of ability to glycosylate FGF23." FT /evidence="ECO:0000269|PubMed:31932717" FT CONFLICT 481 FT /note="Q -> R (in Ref. 1; CAA63371)" FT /evidence="ECO:0000305" SQ SEQUENCE 633 AA; 72610 MW; 3019B2DCCC19A584 CRC64; MAHLKRLVKL HIKRHYHKKF WKLGAVIFFF IIVLVLMQRE VSVQYSKEES RMERNMKNKN KMLDLMLEAV NNIKDAMPKM QIGAPVRQNI DAGERPCLQG YYTAAELKPV LDRPPQDSNA PGASGKAFKT TNLSVEEQKE KERGEAKHCF NAFASDRISL HRDLGPDTRP PECIEQKFKR CPPLPTTSVI IVFHNEAWST LLRTVHSVLY SSPAILLKEI ILVDDASVDE YLHDKLDEYV KQFSIVKIVR QRERKGLITA RLLGATVATA ETLTFLDAHC ECFYGWLEPL LARIAENYTA VVSPDIASID LNTFEFNKPS PYGSNHNRGN FDWSLSFGWE SLPDHEKQRR KDETYPIKTP TFAGGLFSIS KEYFEYIGSY DEEMEIWGGE NIEMSFRVWQ CGGQLEIMPC SVVGHVFRSK SPHSFPKGTQ VIARNQVRLA EVWMDEYKEI FYRRNTDAAK IVKQKAFGDL SKRFEIKHRL QCKNFTWYLN NIYPEVYVPD LNPVISGYIK SVGQPLCLDV GENNQGGKPL IMYTCHGLGG NQYFEYSAQH EIRHNIQKEL CLHAAQGLVQ LKACTYKGHK TVVTGEQIWE IQKDQLLYNP FLKMCLSANG EHPSLVSCNP SDPLQKWILS QND //